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Both Drosophila matrix metalloproteinases have released and membrane-tethered forms but have different substrates

Kimberly S LaFever1,2,3, Xiaoxi Wang1,2,3, Patrick Page-McCaw4

  • 1Dept. of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN, USA.

Scientific Reports
|March 17, 2017
PubMed

Insights

Drosophila matrix metalloproteinases (MMPs) are not distinguished by location. Both DmMmp1 and DmMmp2 are secreted and cell-surface bound, with GPI-anchors, and cleave distinct substrates, clarifying MMP specificity.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • Matrix metalloproteinases (MMPs) are crucial extracellular proteases involved in tissue remodeling and signaling.
  • Vertebrate MMPs present challenges in specificity studies due to large numbers, overlapping substrates, and genetic redundancy.
  • Drosophila melanogaster offers a simplified model with only two MMP genes (DmMmp1, DmMmp2) for studying MMP specificity.

Purpose of the Study:

  • To investigate the localization and function of Drosophila MMPs (DmMmp1 and DmMmp2).
  • To determine the basis of substrate specificity within the limited Drosophila MMP family.
  • To clarify the role of protein localization and anchoring in MMP function.

Main Methods:

  • Utilized new reagents and assays to analyze Drosophila MMPs.
  • Investigated protein localization (cell surface vs. secreted) and anchoring (GPI-anchors).
  • Assessed MMP activity and substrate cleavage profiles.

Main Results:

  • Both DmMmp1 and DmMmp2 are found at the cell surface and secreted into media.
  • Products of both genes possess GPI-anchors.
  • Inactive, GPI-anchored MMPs were found to promote cell adhesion.
  • DmMmp1 and DmMmp2 cleave distinct substrates, indicating functional divergence.

Conclusions:

  • Protein localization is not the primary determinant of specificity between DmMmp1 and DmMmp2.
  • GPI-anchoring and substrate cleavage are key factors in Drosophila MMP specificity.
  • Drosophila MMPs provide a valuable model for understanding fundamental principles of protease function and specificity.

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